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Overview

Uniprot ID	P34058
Protein Name	Heat shock protein HSP 90-beta
Gene Name	Hsp90ab1
Organism	Rattus norvegicus

Kla Sites from experimental identification

Position	Flanking peptide
107	NNLGTIAKSGTKAFM
180	EPIGRGTKVILHLKE
186	TKVILHLKEDQTEYL
275	KTKKIKEKYIDQEEL
284	IDQEELNKTKPIWTR
286	QEELNKTKPIWTRNP
347	PFDLFENKKKKNNIK
354	KKKKNNIKLYVRRVF
399	REMLQQSKILKVIRK
438	EAFSKNLKLGIHEDS
481	SRMKETQKSIYYITG
53	NASDALDKIRYESLT
531	QLKEFDGKSLVSVTK
538	KSLVSVTKEGLELPE
559	KMEESKAKFENLCKL
568	ENLCKLMKEILDKKV
577	ILDKKVEKVTISNRL
607	ANMERIMKAQALRDN
624	MGYMMAKKHLEINPD
64	ESLTDPSKLDSGKEL

Function

Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself. Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone. After the completion of the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle. Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. HSP90 and its co-chaperones modulate transcription at least at three different levels. They first alter the steady-state levels of certain transcription factors in response to various physiological cues. Second, they modulate the activity of certain epigenetic modifiers, such as histone deacetylases or DNA methyl transferases, and thereby respond to the change in the environment. Third, they participate in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression. Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation. Promotes cell differentiation by chaperoning BIRC2 and thereby protecting from auto-ubiquitination and degradation by the proteasomal machinery. Main chaperone involved in the phosphorylation/activation of the STAT1 by chaperoning both JAK2 and PRKCE under heat shock and in turn, activates its own transcription. Involved in the translocation into ERGIC (endoplasmic reticulum-Golgi intermediate compartment) of leaderless cargos (lacking the secretion signal sequence) such as the interleukin 1/IL-1; the translocation process is mediated by the cargo receptor TMED10

Protein Sequence

10 MPEEVHHGEE 20 EVETFAFQAE 30 IAQLMSLIIN 40 TFYSNKEIFL 50 RELISNASDA 60 LDKIRYESLT 70 DPSKLDSGKE 80 LKIDIIPNPQ 90 ERTLTLVDTG 100 IGMTKADLIN 110 NLGTIAKSGT 120 KAFMEALQAG 130 ADISMIGQFG 140 VGFYSAYLVA 150 EKVVVITKHN 160 DDEQYAWESS 170 AGGSFTVRAD 180 HGEPIGRGTK 190 VILHLKEDQT 200 EYLEERRVKE 210 VVKKHSQFIG 220 YPITLYLEKE 230 REKEISDDEA 240 EEEKGEKEEE 250 DKEDEEKPKI 260 EDVGSDEEDD 270 SGKDKKKKTK 280 KIKEKYIDQE 290 ELNKTKPIWT 300 RNPDDITQEE 310 YGEFYKSLTN 320 DWEDHLAVKH 330 FSVEGQLEFR 340 ALLFIPRRAP 350 FDLFENKKKK 360 NNIKLYVRRV 370 FIMDSCDELI 380 PEYLNFIRGV 390 VDSEDLPLNI 400 SREMLQQSKI 410 LKVIRKNIVK 420 KCLELFSELA 430 EDKENYKKFY 440 EAFSKNLKLG 450 IHEDSTNRRR 460 LSELLRYHTS 470 QSGDEMTSLS 480 EYVSRMKETQ 490 KSIYYITGES 500 KEQVANSAFV 510 ERVRKRGFEV 520 VYMTEPIDEY 530 CVQQLKEFDG 540 KSLVSVTKEG 550 LELPEDEEEK 560 KKMEESKAKF 570 ENLCKLMKEI 580 LDKKVEKVTI 590 SNRLVSSPCC 600 IVTSTYGWTA 610 NMERIMKAQA 620 LRDNSTMGYM 630 MAKKHLEINP 640 DHPIVETLRQ 650 KAEADKNDKA 660 VKDLVVLLFE 670 TALLSSGFSL 680 EDPQTHSNRI 690 YRMIKLGLGI 700 DEDEVTAEEP 710 SAAVPDEIPP 720 LEGDEDASRM EEVD

Gene Ontology

Classification	GO ID	Description
Molecular Function	GO:0042826	histone deacetylase binding
Cellular Component	GO:0016324	apical plasma membrane
Cellular Component	GO:0034751	aryl hydrocarbon receptor complex
Cellular Component	GO:0044295	axonal growth cone
Cellular Component	GO:0016323	basolateral plasma membrane
Cellular Component	GO:0031526	brush border membrane
Cellular Component	GO:0009986	cell surface
Cellular Component	GO:0008180	COP9 signalosome
Cellular Component	GO:0005737	cytoplasm
Cellular Component	GO:0005829	cytosol
Cellular Component	GO:0044294	dendritic growth cone
Cellular Component	GO:0120293	dynein axonemal particle
Cellular Component	GO:0005576	extracellular region
Cellular Component	GO:1990565	HSP90-CDC37 chaperone complex
Cellular Component	GO:0016234	inclusion body
Cellular Component	GO:0043202	lysosomal lumen
Cellular Component	GO:0005765	lysosomal membrane
Cellular Component	GO:0042470	melanosome
Cellular Component	GO:0043025	neuronal cell body
Cellular Component	GO:0005634	nucleus
Cellular Component	GO:1990917	ooplasm
Cellular Component	GO:0048471	perinuclear region of cytoplasm
Cellular Component	GO:0005886	plasma membrane
Cellular Component	GO:0101031	protein folding chaperone complex
Cellular Component	GO:0032991	protein-containing complex
Cellular Component	GO:1990913	sperm head plasma membrane
Molecular Function	GO:0005524	ATP binding
Molecular Function	GO:0016887	ATP hydrolysis activity
Molecular Function	GO:0043008	ATP-dependent protein binding
Molecular Function	GO:0140662	ATP-dependent protein folding chaperone
Molecular Function	GO:0002135	CTP binding
Molecular Function	GO:0032564	dATP binding
Molecular Function	GO:0097718	disordered domain specific binding
Molecular Function	GO:0070182	DNA polymerase binding
Molecular Function	GO:0003725	double-stranded RNA binding
Molecular Function	GO:0005525	GTP binding
Molecular Function	GO:0031072	heat shock protein binding
Molecular Function	GO:1901363	heterocyclic compound binding
Molecular Function	GO:1990226	histone methyltransferase binding
Molecular Function	GO:0042802	identical protein binding
Molecular Function	GO:0019900	kinase binding
Molecular Function	GO:0042277	peptide binding
Molecular Function	GO:0140597	protein carrier chaperone
Molecular Function	GO:0046983	protein dimerization activity
Molecular Function	GO:0044183	protein folding chaperone
Molecular Function	GO:0042803	protein homodimerization activity
Molecular Function	GO:0019901	protein kinase binding
Molecular Function	GO:0072542	protein phosphatase activator activity
Molecular Function	GO:0141069	receptor ligand inhibitor activity
Molecular Function	GO:0017098	sulfonylurea receptor binding
Molecular Function	GO:0048156	tau protein binding
Molecular Function	GO:0044325	transmembrane transporter binding
Molecular Function	GO:0031625	ubiquitin protein ligase binding
Molecular Function	GO:0051082	unfolded protein binding
Molecular Function	GO:0002134	UTP binding
Biological Process	GO:0034605	cellular response to heat
Biological Process	GO:0071353	cellular response to interleukin-4
Biological Process	GO:0061684	chaperone-mediated autophagy
Biological Process	GO:0051131	chaperone-mediated protein complex assembly
Biological Process	GO:0043066	negative regulation of apoptotic process
Biological Process	GO:1903660	negative regulation of complement-dependent cytotoxicity
Biological Process	GO:0043524	negative regulation of neuron apoptotic process
Biological Process	GO:1901799	negative regulation of proteasomal protein catabolic process
Biological Process	GO:0032435	negative regulation of proteasomal ubiquitin-dependent protein catabolic process
Biological Process	GO:0001890	placenta development
Biological Process	GO:0045597	positive regulation of cell differentiation
Biological Process	GO:0045793	positive regulation of cell size
Biological Process	GO:0042307	positive regulation of protein import into nucleus
Biological Process	GO:2000010	positive regulation of protein localization to cell surface
Biological Process	GO:0071902	positive regulation of protein serine/threonine kinase activity
Biological Process	GO:0030511	positive regulation of transforming growth factor beta receptor signaling pathway
Biological Process	GO:0006457	protein folding
Biological Process	GO:0050821	protein stabilization
Biological Process	GO:0051726	regulation of cell cycle
Biological Process	GO:0061635	regulation of protein complex stability
Biological Process	GO:0032880	regulation of protein localization
Biological Process	GO:0031396	regulation of protein ubiquitination
Biological Process	GO:0042220	response to cocaine
Biological Process	GO:0009651	response to salt stress
Biological Process	GO:0006986	response to unfolded protein
Biological Process	GO:0009410	response to xenobiotic stimulus
Biological Process	GO:0097435	supramolecular fiber organization
Biological Process	GO:1905323	telomerase holoenzyme complex assembly
Biological Process	GO:0007004	telomere maintenance via telomerase
Biological Process	GO:0019062	virion attachment to host cell

Reference

[1] Sheng L, Xu H, Wang Y, Ni J, Xiang T et al.. Systematic analysis of lysine lactylation in nucleus pulposus cells.. iScience 27(11):111157. 2024 Nov 15. PMID: 39524337.

[2] Chen Y, Sun W, Sun Z, Zhao H, Wu T et al.. Effect of electroacupuncture on hippocampal protein lactylation in a rat model of vascular dementia.. Front Neurol 16:1629474. 2025. PMID: 40963935.